# HIST2H2AC

> Mediated Wiki article. Canonical URL: https://mediated.wiki/source/HIST2H2AC
> Markdown URL: https://mediated.wiki/source/HIST2H2AC.md
> Source: https://en.wikipedia.org/wiki/HIST2H2AC
> Source revision: 1301322749
> License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/)

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Histone H2A type 2-C''' is a [protein](/source/protein) that in humans is encoded by the ''HIST2H2AC'' [gene](/source/gene).<ref name="pmid1469070">{{cite journal |vauthors=Collart D, Romain PL, Huebner K, Pockwinse S, Pilapil S, Cannizzaro LA, Lian JB, Croce CM, Stein JL, Stein GS | title = A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing | journal = J Cell Biochem | volume = 50 | issue = 4 | pages = 374–85 |date=Jan 1993 | pmid = 1469070 | doi = 10.1002/jcb.240500406 | s2cid = 7732783 }}</ref><ref name="pmid9439656">{{cite journal |vauthors=Albig W, Doenecke D | title = The human histone gene cluster at the D6S105 locus | journal = Hum Genet | volume = 101 | issue = 3 | pages = 284–94 |date=Feb 1998 | pmid = 9439656 | doi =10.1007/s004390050630  | s2cid = 38539096 }}</ref><ref name="pmid12408966">{{cite journal |vauthors=Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ | title = The human and mouse replication-dependent histone genes | journal = Genomics | volume = 80 | issue = 5 | pages = 487–98 |date=Oct 2002 | pmid = 12408966 | doi =10.1016/S0888-7543(02)96850-3  }}</ref><ref name="entrez"/>

[Histones](/source/Histones) are basic [nuclear proteins](/source/nuclear_proteins) that are responsible for the [nucleosome](/source/nucleosome) structure of the chromosomal fiber in [eukaryotes](/source/eukaryotes). Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an [octamer](/source/octamer), around which approximately 146 bp of [DNA](/source/DNA) is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of [chromatin](/source/chromatin) into higher order      structures. This gene is [intronless](/source/intronless) and encodes a member of the histone H2A family.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2AC histone cluster 2, H2ac| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8338}}</ref>

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal  |vauthors=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535–44 |year= 1998 |pmid= 9566873 |doi=  10.1128/mcb.18.5.2535| pmc=110633  }}
*{{cite journal  |vauthors=Kimura A, Horikoshi M |title=Tip60 acetylates six lysines of a specific class in core histones in vitro |journal=Genes Cells |volume=3 |issue= 12 |pages= 789–800 |year= 1999 |pmid= 10096020 |doi=10.1046/j.1365-2443.1998.00229.x  |doi-access=free }}
*{{cite journal   |vauthors=Deng L, de la Fuente C, Fu P, etal |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones |journal=Virology |volume=277 |issue= 2 |pages= 278–95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 |doi-access= free }}
*{{cite journal   |vauthors=Deng L, Wang D, de la Fuente C, etal |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA |journal=Virology |volume=289 |issue= 2 |pages= 312–26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 |doi-access= free }}
*{{cite journal   |vauthors=Chen A, Kleiman FE, Manley JL, etal |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085–92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200 |doi-access= free }}
*{{cite journal   |vauthors=Lahn BT, Tang ZL, Zhou J, etal |title=Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 13 |pages= 8707–12 |year= 2002 |pmid= 12072557 |doi= 10.1073/pnas.082248899  | pmc=124363 |bibcode=2002PNAS...99.8707L |doi-access=free }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Yoon HG, Chan DW, Huang ZQ, etal |title=Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1 |journal=EMBO J. |volume=22 |issue= 6 |pages= 1336–46 |year= 2003 |pmid= 12628926 |doi= 10.1093/emboj/cdg120  | pmc=151047 }}
*{{cite journal   |vauthors=Fujita K, Shimazaki N, Ohta Y, etal |title=Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone |journal=Genes Cells |volume=8 |issue= 6 |pages= 559–71 |year= 2004 |pmid= 12786946 |doi=10.1046/j.1365-2443.2003.00656.x  |s2cid=25223336 |doi-access=free }}
*{{cite journal  |vauthors=Lusic M, Marcello A, Cereseto A, Giacca M |title=Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter |journal=EMBO J. |volume=22 |issue= 24 |pages= 6550–61 |year= 2004 |pmid= 14657027 |doi= 10.1093/emboj/cdg631  | pmc=291826 }}
*{{cite journal  |vauthors=Zhang Y, Griffin K, Mondal N, Parvin JD |title=Phosphorylation of histone H2A inhibits transcription on chromatin templates |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 21866–72 |year= 2004 |pmid= 15010469 |doi= 10.1074/jbc.M400099200 |doi-access=free  }}
*{{cite journal   |vauthors=Aihara H, Nakagawa T, Yasui K, etal |title=Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo |journal=Genes Dev. |volume=18 |issue= 8 |pages= 877–88 |year= 2004 |pmid= 15078818 |doi= 10.1101/gad.1184604  | pmc=395847 }}
*{{cite journal   |vauthors=Wang H, Wang L, Erdjument-Bromage H, etal |title=Role of histone H2A ubiquitination in Polycomb silencing |journal=Nature |volume=431 |issue= 7010 |pages= 873–8 |year= 2004 |pmid= 15386022 |doi= 10.1038/nature02985 |bibcode=2004Natur.431..873W |s2cid=4344378 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal   |vauthors=Braastad CD, Hovhannisyan H, van Wijnen AJ, etal |title=Functional characterization of a human histone gene cluster duplication |journal=Gene |volume=342 |issue= 1 |pages= 35–40 |year= 2005 |pmid= 15527963 |doi= 10.1016/j.gene.2004.07.036 }}
*{{cite journal  |vauthors=Hagiwara T, Hidaka Y, Yamada M |title=Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes |journal=Biochemistry |volume=44 |issue= 15 |pages= 5827–34 |year= 2005 |pmid= 15823041 |doi= 10.1021/bi047505c }}
*{{cite journal   |vauthors=Bonenfant D, Coulot M, Towbin H, etal |title=Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry |journal=Mol. Cell. Proteomics |volume=5 |issue= 3 |pages= 541–52 |year= 2006 |pmid= 16319397 |doi= 10.1074/mcp.M500288-MCP200 |doi-access= free }}
{{refend}}
{{PDB Gallery|geneid=8338}}

{{gene-1-stub}}

---
Adapted from the Wikipedia article [HIST2H2AC](https://en.wikipedia.org/wiki/HIST2H2AC) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/HIST2H2AC?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.